Enzymes

• biological catalysts

• speed up reactions so that the reactions happen at normal body temperature

• globular proteins with tertiary or quaternary structure

Substrate

• reactant

• 2 substrates forming 1 product or 1 substrate forming 2 products

• catabolic or anabolic metabolism

Active Site

• specific shape with active site in enzyme

• region of enzyme where substrate will bond and reaction will occur

• reaction will occur here

• chemical attraction between AS and enzyme

• enzyme and substrate is like lock and key

Denaturation

• enzyme loses conformation and can't function

• separate 2 DNA strands

• extreme conditions of pH, salt concentration, and temperature cause this catalyst change reaction rate without being consumed

Immobilized Enzymes

• in industry

• restrict enzyme movement

• commercial use of 500+ enzymes

• more stable

• uses biotechnology

Biotechnology

• makes products like laundry detergent, textile preparation, biodegradable clothing

• normal production of lactase, which breaks lactose into glucose and galactose

• makes yeast, which makes lactase

• helps in lactose intolerance

3 steps in catalysis

1. Substrate(s) bond to active site (s)

2. Substrate turns to a product bound to the enzyme

3. Active Site releases the product and can catalyze other substances

Substrate Movement

• random movement in water

• substrate smaller and faster than enzyme

• random movement causes collision which causes enzyme-catalyzed reaction

Enzymes & Temperature

• temperature increase causes enzyme efficiency to increase until a certain point

• once that point is crossed, the enzyme denatures

Enzymes & pH

• optimum pH of 7

• activity level reduced with pH change

Enzymes & Substrate Concentration

• directly proportional

• until all enzymes are active

• then no effect on concentration

Cofactors

• nonprotein enzyme helpers

• inorganic or organic

• organic includes coenzymes

• coenzymes include vitamins

Enzyme Inhibitors

• slow down enzyme reaction rate

• competitive or noncompetitive

• ex. toxin, poison, pesticides, antibiotics

Competitive Inhibitor

• binds to enzyme's active site

• directly competes with the substrate

Competitive Inhibitor Graph

• same Vmax

• lower Km

Noncompetitive Inhibitor

• binds to other part of enzyme

• denatures it, making it less useful

• same Km, lower Vmax

Noncompetitive Inhibitor Graph

• same Km

• lower Vmax

Enzyme Regulation

• chemical chaos if cell's metabolic pathways weren't tightly regulated

• cells switch genes encoding certain enzymes on and off or regulating enzyme activity

Allosteric Regulation

• inhibit or stimulate enzyme

• regulatory molecule binds to enzyme at one site and affects action at another

Allosteric Regulation & Inhibition

• most allosteric-regulated enzymes made from polypeptide subunits

• active and inactive forms

• activator binding and inhibitor binding

Activator binding site

• stabilizes the active form of the enzyme

Inhibitor Binding Site

• stabilizes enzyme's inactive form

Feedback Inhibition

• end-product of metabolic pathway shuts down the pathway

• prevents a cell from wasting chemical resources by synthesizing extra product

Assumption of a Steady State

• transient phase where ES concentration does not change during the reaction (dES/dt) = 0 Km

• substrate concentration where V0 = (1/2) (Vmax)

Enzyme classification

• uses a number system

Enzyme Classes

• Oxidoreductase

  • transfer electrons in Redox reactions to catalyze oxidation or reduction

  • oxidation

    • reduction in electrons

    • increase oxidation state

  • reduction

    • increase in electrons

    • decrease oxidation state

• Transferase

  • transfer functional groups between molecules

• Hydrolase

  • break bonds by adding H2O

• Lyase

  • elimination reactions to form double bonds

  • remove hydrogen and carbon

• Isomerase

  • aka utase

  • intramolecular arrangements

  • one of the "weirder" enzymes

• Ligase

  • join molecules with new bonds metabolism

  • total of organism's chemical reactions

  • emergent property from cellular molecule interactions

Metabolic Pathway

• begins with a specific molecule and ends with a product

• chain of reactions

• enzymes catalyze each step

Catabolic pathways

• release energy by breaking down complex molecules into simpler ones

• ex. cellular respiration

Anabolic Pathways

• use energy to build complex molecules from simpler ones

• ex. protein synthesis from amino acids

Bioenergetics

• the study of how organisms manage their energy resources

Energy

• the capacity to cause change

• exists in various forms

• some forms can perform work

Kinetic energy

• energy associated with motion

• Heat (thermal energy)

• kinetic energy

  • associated with the random movement of atoms of molecules

Potential Energy

• energy that matter possesses because of its location or structure

Chemical Energy

• potential energy available for release in a chemical reaction

Thermodynamics

• the study of energy transformations

Isolated System

• isolated from its surroundings

• ex. liquid in a thermos

Open System

• energy and matter can be transferred between the system and its surroundings

• ex. organisms

First Law of Thermodynamics

• energy of the universe is constant

• energy can't be created or destroyed, only changed

• principle of conservation of energy

Second Law of Thermodynamics

• during every energy transfer or transformation, some energy is unusable, and is often lost as heat

• each change increases the entropy (disorder) of the universe

Spontaneous Processes

• occur without energy input

• they can happen quickly or slowly

• increase entropy of the universe

Biological Order and Disorder

• cells create ordered structures from less ordered materials

• organisms replaced ordered forms of matter and energy with less ordered forms

• energy flows into an ecosystem as light and out as heat

Exergonic Reaction

• net release of free energy

• spontaneous

Endergonic Reaction

• absorbs free energy from its surroundings

• nonspontaneous